Our group studies the composition and molecular architecture of protein complexes involved in central metabolism in Actinobacteria, and the signaling pathways and/or allosteric mechanisms that contribute to their regulation. The objective is to shed light on the mechanisms that underlie the metabolic plasticity of the members of this phylum. Our experimental approaches involve the integrative structural biology of large metabolic complexes from the non-pathogenic species Corynebacterium glutamicum, a well-known workhorse for the biotech industry, but we are also interested in structural enzymology for drug design purposes, especially for targets from Mycobacterium tuberculosis. More information about our current activities can be found on the SUPERCPLX and METACTINO project pages.
Acyl-CoAs are the major metabolic carriers of carbon in living organisms. The most conserved ways to their synthesis include the oxidative decarboxylation of α-ketoacids carried out by three distinct enzymatic machineries: the pyruvate dehydrogenase […]
Tuberculosis still remains a major threat for public health, with one-third of the world population latently infected, and more than one million deaths per year according to the WHO. Among the factors that have […]
Despite the conservation of central metabolism, an increasing amount of evidence indicates that there are unique features in Actinobacteria, one of the largest bacterial phyla that includes important human pathogens like Mycobacterium tuberculosis and […]
2019Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling., Sci Signal 2019 05; 12(580): .
2019Novel mechanistic insights into physiological signaling pathways mediated by mycobacterial Ser/Thr protein kinases., Genes Immun 2019 05; 20(5): 383-393.
2019New substrates and interactors of the mycobacterial Serine/Threonine protein kinase PknG identified by a tailored interactomic approach., J Proteomics 2019 02; 192(): 321-333.
2017PknG senses amino acid availability to control metabolism and virulence of Mycobacterium tuberculosis, PLoS Pathog. 2017 May;13(5):e1006399.
2017The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation, FEBS J. 2017 02;284(4):602-614.
2015Thiophenecarboxamide Derivatives Activated by EthA Kill Mycobacterium tuberculosis by Inhibiting the CTP Synthetase PyrG, Chem. Biol. 2015 Jul;22(7):917-27.
2015The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation, Proteins 2015 May;83(5):982-8.
2014A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase), Biochem. J. 2014 Feb;457(3):425-34.
2013GarA is an essential regulator of metabolism in Mycobacterium tuberculosis, Mol. Microbiol. 2013 Oct;90(2):356-66.
2011Functional plasticity and allosteric regulation of α-ketoglutarate decarboxylase in central mycobacterial metabolism, Chem. Biol. 2011 Aug;18(8):1011-20.
2008Regulation of glutamate metabolism by protein kinases in mycobacteria, Mol. Microbiol. 2008 Dec;70(6):1408-23.
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